{Reference Type}: Journal Article
{Title}: A Rhodanese-Like Enzyme that Catalyzes Desulfination of Ergothioneine Sulfinic Acid.
{Author}: Nalivaiko EY;Seebeck FP;
{Journal}: Chembiochem
{Volume}: 25
{Issue}: 9
{Year}: 2024 May 2
{Factor}: 3.461
{DOI}: 10.1002/cbic.202400131
{Abstract}: Many actinobacterial species contain structural genes for iron-dependent enzymes that consume ergothioneine by way of O2-dependent dioxygenation. The resulting product ergothioneine sulfinic acid is stable under physiological conditions unless cleavage to sulfur dioxide and trimethyl histidine is catalyzed by a dedicated desulfinase. This report documents that two types of ergothioneine sulfinic desulfinases have evolved by convergent evolution. One type is related to metal-dependent decarboxylases while the other belongs to the superfamily of rhodanese-like enzymes. Pairs of ergothioneine dioxygenases (ETDO) and ergothioneine sulfinic acid desulfinase (ETSD) occur in thousands of sequenced actinobacteria, suggesting that oxidative ergothioneine degradation is a common activity in this phylum.